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Updated: Nov 20, 2025

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption
Hyun Ji Ha1, Hye Lin Chun1,2, So Yeon Lee1,2
1College of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea.
Abstract:
Immunity-related GTPase B10 (IRGB10) belongs to the interferon (IFN)-inducible GTPases, a family of proteins critical to host defense. It is induced by IFNs after pathogen infection, and plays a role in liberating pathogenic ligands for the activation of the inflammasome by directly disrupting the pathogen membrane. Although IRGB10 has been intensively studied owing to its functional importance in the cell-autonomous immune response, the molecular mechanism of IRGB10-mediated microbial membrane disruption is still unclear. In this study, we report the structure of mouse IRGB10. Our structural study showed that IRGB10 bound to GDP forms an inactive head-to-head dimer. Further structural analysis and comparisons indicated that IRGB10 might change its conformation to activate its membrane-binding and disruptive functions. Based on this observation, we propose a model of the working mechanism of IRGB10 during pathogen membrane disruption.
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